Possibly the human body's most infamous protein, P53 is mutated in 50% of all cancers. That's right, TP53 (the gene that encodes P53 protein) is cancer's most mutated gene!
P53 is a tumor suppressor, meaning it protects cells from becoming cancerous. In times of genotoxic and cellular stress, P53 activates cellular pathways that promote DNA repair, cell-cycle arrest, and cell death (killing off dangerous and damaged cells). If P53 is defective, the opposite occurs. Cells don't repair DNA appropriately, causing genetic mutations. Cells don't undergo cell death, allowing malfunctioning cells to survive and propagate. And cells don't stop dividing, enabling uncontrolled cellular growth that contributes to tumor formation.
In a nutshell, P53 is a good guy; he's the guardian of the genome. But if he becomes mutated, P53's hero status gets demoted. Mutant P53 presents quite the challenge for cancer biologists. Can P53's hero status be medicinally reinstated? Well — yes! We can reactivate P53 to guard the genome again. Two strategies to bolster P53's hero status have been quite successful in recent years and are setting the stage for a new class of chemotherapies:
1. Inhibiting MDM2, P53's sworn enemy
The P53 protein can be tagged with a small protein called ubiquitin, signaling P53 for degradation. P53 ubiquitination is a healthy, normal event in our cells to sustain P53 at an appropriate level (too much of a good thing can be a bad thing). However, if P53 is deficient, we don't need P53 to be ubiquitinated as frequently. So, scientists have developed inhibitors for MDM2, the protein responsible for P53 ubiquitination and destruction. By blocking MDM2, P53 is not ubiquitinated, and P53 levels in the cell rise, allowing deficient P53 the extra help to do its job.
Seven MDM2 inhibitors are currently in clinical trials for various cancers, and a few have even progressed to phase III trials!
Note: MDM2 isn't the only protein that regulates P53 levels in the cell. Other proteins for this pathway are also chemotherapeutic targets.
2. A direct approach: P53 activators
Most P53 mutants are deficient in the DNA binding domain. If the DNA binding domain is unstable, the protein can't bind DNA and jumpstart the cellular pathways needed for cell death, DNA repair, and cell division arrest.
Scientists have designed small molecule activators that bind P53 and restore the structure of the DNA binding domain, allowing P53 to bind DNA and initiate gene expression. Two small-molecule activators are now in clinical trials and seem promising thus far. COTI-2 is undergoing stage II clinical trials for various cancers, while APR-246 has made it to stage three for blood cancers!
P53 activators aren't approved yet, nor is their approval for clinical use guaranteed. But the fact that P53 activators are in clinical trials, especially stage three, is a remarkable accomplishment by the scientific community! P53 is the holy grail of chemotherapeutic targets. With so many cancers harboring P53 mutations the therapeutic reach of these activators is substantial. There was a time when P53 was considered undruggable, an impossible chemotheraputic target.
P53 activation is no longer a fantasy. Unlike Marvel movies and comic books, P53 reactivation is a reality.
*Reposted from 09/11/20
So, it's your first year of grad school — congrats! But your first year is during a pandemic — yikes! Graduate school is stressful enough without having to worry about a deadly virus. Hopefully, this post will help you navigate through your first year by providing concrete advice for choosing your new lab and acclimating to a new workspace.
As a first-year STEM student, your school likely requires you to conduct research in various labs (usually 2-4) for a temporary period of time. After these rotations are complete, you will choose a lab as your new home for the next 4-7 years! It's an important choice to make, and you aren't alone if this process brings about some anxiety. Here are 10 tips to help ensure you arrive at the right decision.
1. Keep an open mind. You might arrive at your school with a PI or research topic in mind. Unfortunately, there are many factors at play that dictate what you will research other than your preferences. Have a Plan B and C just in case Plan A is not in your cards.
2. Shrink that chip on your shoulder. Its tempting to show-off and be over-competitive with your new lab mates. Don't. It's an awful way to make new friends. To be blunt here, your new co-workers don't care how smart you are. They want a lab-mate who is a hard-worker and helpful to work alongside. Be yourself. Save the energy you would spend on trying to impress others to do well at the tasks at hand.
3. Remember why you are there. The purpose of a rotation is to test out a lab. You are not there to churn out data, work long weeks, and publish a paper in a short amount of time. If you feel anxious or overworked during a rotation, imagine what five years in that lab will be like.
4. Ditch the "that's not how my old lab did it." saying. Your new lab will do things in new ways, and there might be a reason for that. When starting work in a new place, it's easy to get caught up in comparisons to the past. But this is a fresh start, embrace the changes and be willing to learn from your new lab-mates and mentors.
5. Ask about funding. $$$$. This point cannot be stressed enough. Just because a PI is taking on rotation students does not mean they have funding to bring you on as a full-time student. Before rotating with a PI, ask if they have money to cover your stipend. If they do not, consider rotating elsewhere. If a PI does not directly answer this question, they might be baiting you to get free labor.
6. Discuss potential thesis topics. Many labs treat students as employees. The students produce data like lab techs, and the thesis is an afterthought. Labs with this mindset are reluctant to let students graduate because they are precious cheap labor. It's important to have research expectations outlined before joining the lab as a student.
7. Speak to other students and faculty in the department. Check-in with others to learn about the reputation of the lab.
8. Ask about time off. Trust me; you need time off. The ideal answer to this question is, "of course, you can take vacations, just communicate with me first." Inquiring about vacation time is an imperative question if your family does not live nearby. Ideally, you should be able to take time off around the holidays and also have personal vacations.
9. Ask about the work schedule. Some labs have strict schedules; others are come and go. Your PI should not demand or coerce you to work more than 40 hours/week. Overtime is your choice.
10. Discuss career development with your PI. It's helpful to have a PI who is also a mentor. Are they invested in your success? Do they support you taking time off for career development? Are they open-minded to non-academic careers? A "no" to any of these questions is concerning.
Lastly, look out for the following Red flags. Any of these behaviors are serious and should not go ignored.
Does the perfect lab exist … hmmm …. perhaps not. Even if you are careful in choosing a lab, you may find yourself feeling unsure of your choice in the future. Start building a support system around you now. If a PI puts you in a difficult position, you'll be happy to have a supportive thesis committee and empathetic mentors outside of your lab to advocate for you.
Good luck this year! And as an academic, remember to stay positive and be kind.
If you follow any beauty influencers on social media, you may be familiar with hair vitamins, supplements designed to make your hair grow long and thick. Of course, these influencers already have long and luxurious hair; most are also sporting hair extensions or fillers. Yet, we are lead to believe their lush hair is the result of hair vitamins.
Insta influencers aren’t the most honest source for advice on beauty supplements — recall the skinny tea phase where celebrities advertised laxatives. But perhaps there is some truth to using hair vitamins.
Hair vitamins come in a few brands, so let’s take a look at the ingredients of three common hair vitamins:
Ok, so we have real vitamins in these supplements. Great! But can they give me Kylie-grade hair?
Folate is essential for DNA and protein synthesis, and deficiency can cause hair and nail growth defects. Folate is naturally occurring in leafy veggies, fruits, meats, and grain. Folic acid is a form of folate that can be stored and supplemented in our food. Folic acid fortification of bread and other wheat products is mandated by many countries, including the US and Canada, to combat birth defects caused by folate deficiency. Therefore, if you eat a balanced diet, you likely acquire the necessary folic acid for healthy nail and hair growth and do not need further supplementation.
Zinc aids in protein synthesis, immune function, and cell division and can be found in meat, nuts, beans, fish, and whole grains. The relationship between zinc levels and hair loss is debated, with some studies showing a correlation between zinc levels and hair loss pathologies such as alopecia. Interestingly, zinc pyrithione shampoos seem to improve hair growth, but this is achieved topically due to reduction of oxidation on the scalp. However, there is no evidence to suggest zinc supplementation supports hair growth in individuals without zinc deficiency.
Seeing a pattern here?
Deficiency in several vitamins can cause hair loss, however, supplementation and overconsumption of these vitamins do not guarantee increased hair growth, especially in healthy individuals. Empirical evidence supporting the efficacy of hair vitamins is scarce. A well-balanced diet can easily substitute hair vitamins. So, save your money! This author declares hair vitamins to be pseudo-science.
It's often believed that cancer results from a modern lifestyle, i.e., eating more processed foods, increasing exposure to various radiation sources, and the general fast pace of life. The truth is that the earliest report of cancer, or the disease that later became known as cancer, dates back to around 1600 BC in ancient Egypt. Yes, perhaps the modern lifestyle has increased cancer cases, but it has also provided us with the necessary technology to detect the disease earlier and treat it more effectively. It should also be noted that humans live significantly longer now than a century or two ago, so naturally, the incidence of cancer will increase.
Cancer treatment comprises of three different areas, surgery, radiation, and chemotherapy. However, when you think of a cancer patient, it is the jarring side effects of chemotherapy that come to mind. While there are many resources on the internet to describe the different side effects of chemotherapy and how to deal with them as patients or caregivers, they rarely discuss the mechanisms through which the drugs work.
Cancer arises from a change in the DNA of a single cell that causes it to multiply and grow unchecked. The causes are varied, such as exposure to too much radiation (which is why radiology technicians walk out of the room when taking an X-ray), exposure to chemical carcinogens such as tobacco smoke or asbestos, viruses such as HPV, or copy errors during DNA replication. These events give rise to the same problem: a cell that replicates faster consumes more resources and does not die when it should. And here lies the crux of the problem: cancer cells are not that much different from healthy cells, so anything that kills the cancer cells will likely kill the healthy cells as well. The trick lies in killing the cancer cells faster than the healthy cells.
"Cancer therapy is like beating the dog with a stick to get rid of his fleas."
How to get away with killing cancer
Since cancer cells grow and replicate faster than healthy cells, most anticancer drugs aim to inhibit the replication process. This can be achieved through targeting DNA or proteins related to cell replication, obstructing the metabolism of the cells, or impeding cell division. Some commonly used drugs like oxaliplatin and carboplatin are involved in all three processes and are referred to as cytotoxic compounds.
And now for the kicker: cancer is treated with a combination of the different types of drugs with varying therapeutic mechanisms for specific cancers in different patients. Therefore, each cancer patient receives a cocktail of various medications that have been optimized to treat their particular cancer.
The compound classes that target DNA include alkylating agents, anticancer antibiotics, and some transition metal complexes. These compounds bind directly to the DNA, climbing in between the DNA base pairs or associating with the DNA so that the DNA cannot be replicated. The inability to replicate DNA causes the cancer cell to senesce (stop multiplying) or die.
Interfering with metabolism
Drugs targeting metabolism include antifolates and antimetabolites, which replace compounds in the cell's metabolic cycle. I.e., folic acid is crucial in cell growth and replication, so antifolates take the place of folic acid but do not perform the necessary functions, so the cancer cells are essentially starved.
Blocking cell division
Antimitotic compounds target cell division, and the most used compounds are plant alkaloids such as vincristine and vinblastine. These compounds prevent the formation of microtubules that guide the separation of cells during mitosis. So, if the cells cannot separate, they cannot replicate.
Right on target: creating cancer-cell specific therapies
While the above mentioned compounds are very effective in treating cancer, they do not discriminate between healthy cells and cancer cells, which gives rise to the nasty side effects we have come to associate with cancer treatment. A more recent class of compounds called "targeted therapies" provide more selective interaction with cellular components specific to the cancer cells.
Targeted therapies include:
At the intersection of cytotoxic agents and targeted treatments lies hormone therapies and kinase inhibitors. While they are more selective towards the cancer cells, treatments may still negatively impact the patient.
Hormone therapy can treat hormone-dependent cancers, such as certain types of breast, ovarian and uterine cancers dependent on estrogen and certain types of prostate and testicular cancers dependent on testosterone. By cutting off access to the necessary hormones, the cancer cells are starved of an essential building block. Removing the hormone from the rest of the body also has extensive side effects relating to fertility, secondary sex characteristics, and sexual performance. Still, the side effects are generally less detrimental than other cytotoxic agents.
Kinase inhibitors target kinetic enzymes that contribute to cell growth. Some cancers express more of a particular kinase than healthy cells, while other cancers express a mutated kinase that is specific to the cancer cells. The mutated KRAS has been a holy grail in medicinal chemistry since it is found in numerous high fatality cancers. The development of an inhibitor has long eluded scientists; however, the FDA recently approved a KRAS inhibitor, Lumakras.
And finally, the current buzzword: immunotherapy. Immunotherapy involves using antibodies that bind proteins specific a cancer cell, thereby recruiting the immune system to clear the cancer. Immunotherapy is the most specific chemotherapy available, but since it is so specific, the number of cancers that can be treated are still limited. Personalized treatments come into play here, where a sample of a patient's cancerous tissue is used to develop an antibody for that patient, like designing a key for a specific lock.
Personalized treatments are still highly specialized and expensive pursuits, yet they might become the future of cancer treatment. Immunotherapy also includes the development of cancer vaccines, such as mRNA vaccines targeting KRAS.
For further reading on the topic, I highly recommend the Pulitzer Prize-winning book by Prof. Siddhartha Mukherjee, The Emperor of all Maladies. The book is accessible to scientists and non-scientists alike and does not assume any knowledge in the field of cancer biology. It tells the tale of how theories around cancer evolved and how the current treatments were discovered and refined, all interspersed with gripping tales of the author's own experiences as a practicing oncologist.
Similarly, the National Cancer Institute's website also provides a lot of practical information if you or a loved one is currently busy with cancer treatment and need some guidance.
Hyaluronic acid sells. It’s in serums, moisturizers, and masks. So, does it help our skin? Or is it just a fancy science term used to drum up business?
Hyaluronic acid (HA for short) is a naturally occurring molecule in the extracellular matrix of our cells. HA is a polysaccharide, a chain of sugars. Small and medium length HA promote blood vessel formation and inhibit cell death, while large HA is immunosuppressive and hinders blood vessel formation. HA is found in connective tissues, joints, the eye, and the umbilical cord. However, in the cosmetic world, HA is best known for its ability to bind water molecules within the skin. But that’s not all; HA is an overachiever and also plays a role in fighting free radicals and collagen remodeling.
Clinical trials of topical HA
In theory, hyaluronic acid should be moisturizing and have anti-aging effects. If HA binds and retains water in our skin, it should have a plumping effect that reduces wrinkles.
Fortunately, there is empirical evidence to suggest HA helps with anti-aging. In one study, females aged 30-60 who used a 0.1% HA cream for 60 days experienced increased moisture and elasticity. Decreased wrinkles were only observed in participants who used low molecular weight HA (30, 150 kDa). Another study agrees, stating that topical HA treatment increased elasticity and moisture, and decreased roughness after twice-daily use over 2, 4, and 8 weeks. HA treatment was also most effective with lower molecular weights, citing increased skin penetration.
In addition to topical application, HA can be injected to plump up skin and lips. As mentioned previously, HA is non-toxic and is, therefore, a favored filler method, although, uncommon complications can happen, including infection, vascular injury, allergic reactions, and displacement of filler.
HA is an abundant biomolecule that affects more than just our skin. Research suggests HA is also beneficial for wound healing, bone regeneration, and possibly cancer treatment.
Science or Pseudo:
Thus far, in our science or pseudo series, I'm delighted to say that we are 2 for 2. Both collagen and hyaluronic acid are science-approved cosmetic agents!
Plenty of medicines are protein inhibitors, meaning the drug binds to a protein to block its function. One example of a common inhibitor medication is angiotensin-converting enzyme (ACE) inhibitors used for high blood pressure. ACE is an enzyme in the blood that creates angiotensin II, a molecule responsible for constricting blood vessels. ACE inhibition limits this constriction, alleviating high blood pressure. A second example of an inhibitor medicine is selective serotonin reuptake inhibitors. These drugs bind to serotonin transporters, allowing serotonin (the happy neurotransmitter) to stay in neuronal synapses longer and are therefore used to treat depression.
Old School - Attacking the active site
Both ACE inhibitors and serotonin reuptake inhibitors bind to proteins at their active sites: the central place of function in a protein. ACE inhibitors bind to the catalytic site – the portion of the protein that creates angiotensin II, while serotonin reuptake inhibitors bind and block the channel that serotonin passes through.
It's intuitive that to inhibit an enzyme, a researcher designs a small molecule that binds and directly impedes a protein's active site. This strategy for inhibitor design is favored for a few reasons:
But never fear; scientists are innovative. To increase the number of possible pharmaceutical targets, researchers are designing inhibitors to target a new class of pharmaceutical targets, protein-protein interactions.
New School - Protein-protein interaction inhibitors
Active sites aren't the only essential interface of a protein. Protein interaction interfaces are also necessary for several reasons.
From a protein's point of view, cells are large and confusing places. So, proteins bind to one another to ensure they are in the proper place at the right time to do their jobs. Additionally, proteins are often made of multiple subunits and function similar to a machine. The subunits of these molecular machineries are held together by protein-protein interactions. Therefore, inhibiting a protein-protein interaction can block a protein's function by displacing its localization in the cell or breaking apart a protein complex.
For some time, protein-protein interactions were deemed "undruggable" because, unlike active sites, protein-protein interfaces are large, flat, and hydrophobic. Overall, most protein-protein interfaces have a suboptimal shape and chemistry for small-molecule inhibitors to bind. However, in the last decade, research has shown that although protein-protein inhibitors' design might be taxing, it's certainly possible.
Dealing with the large interfaces
Although protein-protein interfaces are large (averaging 28 amino acids), researchers have found that a small portion of amino acids, termed "hot spots," are responsible for most of the energy required for protein binding. Therefore, the entire protein-protein interface is not the target for site; rather, the hot spot amino acids are.
Struggling with flat target sites
At first glance, most protein-protein interfaces seem flat, but that isn't necessarily the case. Hot spot residues often reside in "pockets" of a protein surface comparable to the size of an active site. And even if it seems hot spots reside on a flat surface, proteins are dynamic, and interfaces may have pockets that appear upon binding to its partner protein.
Combatting the hydrophobicity issue
When it comes to hydrophobic and hydrophilic properties, "like likes like." Hydrophilic molecules bind hydrophilic molecules, while hydrophobic molecules bind hydrophobic molecules. So, a hydrophobic interface will bind hydrophobic inhibitors.
Hydrophobic inhibitors perform poorly in the human body since we are made of mostly water. Therefore, scientists can optimize hydrophobic inhibitors by adding hydrophilic chemical groups to the inhibitor and removing unnecessary hydrophobic groups. And although the core of the protein-protein interaction is often hydrophobic, charged residues often support the interface, which an inhibitor can also target.
Where we stand now
Tirofiban, an integrin disrupter, has earned FDA approval to treat stroke patients. Its mechanism of action is to break apart integrins in the blood and prevent blockages in the brain's blood vessels. Additionally, MDM2-P53 disruptors are undergoing clinical testing for cancer. These inhibitors selectively kill cancer cells by breaking apart the MDM2-P53 interaction. MDM2 inhibits P53, a protein that signals cell death during stress. Stabilizing P53 activity allows P53 to amplify the cell death signal in cancer cells.
Since the strategy for targeting protein-protein interactions is new, few approved drugs target protein-protein interactions. However, the mere fact that some protein-protein inhibitors are undergoing clinical testing is astronomical, considering this class of drugs was once declared impossible. The success of tirofiban and MDM2-P53 inhibitors garners optimism that more protein-protein inhibitors will develop into novel medicine.
Will protein-protein inhibitors replace active site inhibition? Likely not. However, this new class of inhibitors will significantly increase the number of protein targets and hopefully improve our chance of creating new life-saving and life-improving drugs.
This post is a science communication piece derived from my recent review article: "Targeting Protein-Protein Interactions in the DNA Damage Response Pathways for Cancer Chemotherapy" published in RSC Chemical Biology. The information shared here encompasses the first half of the paper. A second post about targeting the DNA Damage Response for cancer chemotherapies is soon to follow.
During the summer, we are keeping summer hours. Posts will be shared bi-weekly and breaks will be taken for the 4th of July, the last two weeks of August, and Labor Day!
Too often, the beauty industry uses pseudoscience to promote its products. Even as a trained scientist, it's difficult to tell the difference between fact, embellishment, and downright fiction.
Further complicating matters, cosmetics do not need FDA approval. Cosmetic regulation by the FDA is minimal, and the laws governing its practice have not changed since 1938. The FDA's power over the cosmetic industry is limited to removing products from the market if they are "adulterated" or "misbranded." In other words, a product can be nixed if it contains a poisonous or spoiled ingredient or if the label provides misleading information.
With the lack of cosmetic regulations, consumers have to ask, "Does this product even work?" Can you trust that charcoal will cleanse your blackheads, that hyaluronic acid will plump your under-eyes, or that collagen will increase the elasticity of your skin?
Today's article will be the beginning of a series of posts on the science of common cosmetic additives. To begin with, we will explore the biology and chemistry of one of skin care's most prevalent ingredients, collagen.
What is Collagen?
Collagen is a natural biomolecule produced by animals, acting as structural support for cells within our connective tissues such as skin, bone, tendons, and cartilage. There are 28 subtypes of collagen, all with similar function.
Collagen is a protein, meaning it's made up of a chain of amino acids folded into a unique shape. Specifically, collagen is made of 3 amino acid chains, twisted together to form a long, helical stretchy protein:
Collagen in skincare
Many biological mechanisms contribute to skin aging, including a decreased production and a deterioration of collagen networks. Intuitively, collagen supplements may alleviate wrinkles and loss of elasticity. But is there scientific evidence to support that collagen is an effective anti-aging additive? Or is an untested theory the driving force of collagen sales?
Quite a few studies support that hydrolyzed collagen has anti-aging effects when used topically. For example, in a 2019 study, participants given topical collagen had increased skin hydration and elasticity in just 28 days, while wrinkles improved after 90 days of treatment. A more recent study also reports topical collagen as an effective cosmetic. Participants who applied a gel containing 1% collagen hydrosolate extracted from chicken stomachs exhibited increased skin hydration and elasticity and decreased wrinkles and roughness. Thus, the collagen flooding the skincare market is, indeed, backed by science!
Side bar: I was inspired to write this blog post when I saw an advertisement for drinkable collagen. I rolled my eyes, convinced it was a ridiculous Instagram trend, similar to skinny teas.
As it turns out, there is validity to ingesting collagen, and quite a few peer-reviewed journal articles back this practice. A study conducted in 2015 reports that middle-aged women who consumed 10 g of collagen per day exhibited increased skin moisture and collagen density. Another study displayed similar results, showing that low-molecular-weight collagen peptide oral supplements increased skin moisture and reduced wrinkles.
Although collagen is synonymous with skincare, collagen plays other pivotal roles in our bodies. In fact, collagen is our most abundant protein. Ongoing research suggests collagen supplementation may assist with bone regeneration, wound healing, and arthritis treatment.
This post is by no means a comprehensive literature review of collagen in skincare. Many additional studies agree with the publications mentioned here. So the next time you reach for a skincare product with collagen, have faith that collagen products aren't so psuedosciency after all.
Bolded Science is on vacation for the month of May. In the meantime...check out some of our older posts.
Considering writing for Bolded Science?
Are you looking to add more writing samples to your sci-comm portfolio? Do you have a science-related cause you'd like to advocate for? Are you conducting super interesting research that you are just dying to tell everyone about? Pitch a blog post to Bolded Science: TheBoldedScientist@gmail.com. It's simple, send an email introducing yourself and 1-2 sentences explaining what you'd like to write about. Then, we will pick a publish date. Once you are approved, write your post and email it 2 weeks before your publish date.
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Thank you to all readers and writers of Bolded Science. This collaborative blog is made possible by our curious, knowledgeable, and passionate community of scientists. In just over a year, Bolded Science has grown to have > 4,000 twitter followers, thousands of blog views, and over 60 blog posts.
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What do you do when you no longer need an item? Unwrapping a Mars bar, what happens to the packaging? How much thought do we put into what we throw away? How much thought do we put into waste overall?
Waste is a big problem, well, actually HUGE. Yes, huge is the right word. National Geographic reports that an estimated 8 million tons of plastic end up in the oceans annually. Furthermore, researchers project that by 2050 the volume of mismanaged plastic waste will climb to 155-256 million metric tons per year. But we are not only talking plastic waste today, so the numbers are even higher!
Where could we possibly hoard all this waste? How can we possibly make all this waste? And how can we get rid of it?
"And then there was waste" - the origins
Definitions for waste:
(a) the useless remains of human activity
(b) materials that are useless to the producer
(c) materials that we are willing to pay to dispose of
In no uncertain terms, waste is the stuff we no longer need and are happy to discard. So, how do we handle waste? Well, categories. Since waste is a megaton problem, knowing its sources and properties can help us understand and deal with it better.
Categories of waste depend on the sources, the two overarching categories are (a) municipal waste and (b) industrial waste. Municipal waste is produced in our private lives, homes, areas of recreation, and activities. On the other hand, industrial waste refers to discarded, emitted, and leftover materials from industrial activities. The division is not always clear. For example, hospitals and restaurants are workplaces for staff but places of health services and recreation for patients and consumers, respectively.
We, as consumers of goods, have control over the waste we produce. We, as industrial teams, can control waste industrially produced. We, as the human race, are responsible for 100% of the waste deposited on the planet. The difference between human waste and animal waste is that our waste cannot be absorbed by nature because of its volume and consistency.
Industrial waste is overwhelmingly more than personal waste. A waste report of the UK (population of around 65 million people) for 2011 accounted for 27,300 thousand tons (27.3 million tons) of municipal waste and 41.1 million tons of industrial waste.
The story these numbers tell us is that for every 100 waste items that the UK produced in 2011, 40 waste items were produced in our private lives, and 60 waste items were produced in our business lives... but in millions of tons.
But recycling — you say?
I hear you. Let's take a quick look. There are many countries with recycling schemes, some of them better than others. However, we do not recycle fast enough, we do not manage waste well enough, and technologies on recycling are still at toddler age.
More effective recycling and management can bring numbers down. And the question remains, where does the waste go? Where do we deposit it?
A game of hide and seek – depositing waste
Deposit sites differ according to geographies, management policies, and laws. However, all countries have landfills to bury waste in the ground. In fact, landfills is the most common way of putting waste out of sight.
Some countries even allow depositing waste directly into water bodies. This practice is not necessarily by design. Rather, lack of legislation to make dumping in water illegal and lack of enforcement of current legislation enables large-scale water pollution. Even when illegal, companies, industries, and businesses still do it. Citizens still do it. Remember when you visited the beach with bags full of snacks? Did you remember to pick up the waste before leaving?
Another "eco-friendly" way to manage waste is incineration – we burn it. Incineration is not a new practice and involves a lot of chemistry and social impact. Incineration is now considered eco-friendly because it is used to produce energy. So we no longer just burn it. We burn it with a purpose. On the flip side, the by-products of incineration may include toxic substances or heavy metals. Ashes and pulp are the end by-product of incineration. Pulp is likely to end up in a landfill.
Take-away message: the Earth has afforded us the grace of not thinking about our waste for a few hundred years now, but we can no longer be as thoughtless. The numbers are daunting. When waste goes out of sight, it doesn't go out of existence. Landfills leak into the ground and poison the soil. Ocean life is obviously in danger from pollution, and the air is fast becoming a concern – think of citizens in industrial cities who wear masks all year round due to poor quality air.
In the current times, the lesson learned is that traditional ways to manage waste have gross negative effects. Despite the research, innovation, and promising new practices, the negative still outweigh the positive. More thoughtfulness of the content in our waste bins is necessary because awareness helps initiate action.